ID   BACH1_MOUSE             Reviewed;         739 AA.
AC   P97302;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   27-MAR-2024, entry version 189.
DE   RecName: Full=Transcription regulator protein BACH1;
DE   AltName: Full=BTB and CNC homolog 1;
GN   Name=Bach1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION
RP   WITH MAFK, AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/cJ;
RX   PubMed=8887638; DOI=10.1128/mcb.16.11.6083;
RA   Oyake T., Itoh K., Motohashi H., Hayashi N., Hoshino H., Nishizawa M.,
RA   Yamamoto M., Igarashi K.;
RT   "Bach proteins belong to a novel family of BTB-basic leucine zipper
RT   transcription factors that interact with MafK and regulate transcription
RT   through the NF-E2 site.";
RL   Mol. Cell. Biol. 16:6083-6095(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NMRI; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-135, AND FUNCTION.
RX   PubMed=19170764; DOI=10.1111/j.1365-2443.2008.01259.x;
RA   Ito N., Watanabe-Matsui M., Igarashi K., Murayama K.;
RT   "Crystal structure of the Bach1 BTB domain and its regulation of
RT   homodimerization.";
RL   Genes Cells 14:167-178(2009).
CC   -!- FUNCTION: Transcriptional regulator that acts as a repressor or
CC       activator, depending on the context (PubMed:8887638, PubMed:19170764).
CC       Binds to NF-E2 DNA binding sites (PubMed:8887638, PubMed:19170764).
CC       Plays important roles in coordinating transcription activation and
CC       repression by MAFK (PubMed:8887638). Together with MAF, represses the
CC       transcription of genes under the control of the NFE2L2 oxidative stress
CC       pathway (By similarity). {ECO:0000250|UniProtKB:O14867,
CC       ECO:0000269|PubMed:19170764, ECO:0000269|PubMed:8887638}.
CC   -!- SUBUNIT: Heterodimer of BACH1 and MAFK.
CC   -!- INTERACTION:
CC       P97302; Q61827: Mafk; NbExp=5; IntAct=EBI-2552417, EBI-15740843;
CC       P97302; P02340: Tp53; NbExp=4; IntAct=EBI-2552417, EBI-474016;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC       ECO:0000269|PubMed:8887638}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:8887638}.
CC   -!- PTM: Ubiquitinated by the SCF(FBXL17) complex, leading to its
CC       degradation by the proteasome. {ECO:0000250|UniProtKB:O14867}.
CC   -!- SIMILARITY: Belongs to the bZIP family. CNC subfamily. {ECO:0000305}.
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DR   EMBL; D86603; BAA13137.1; -; mRNA.
DR   EMBL; BC057894; AAH57894.1; -; mRNA.
DR   CCDS; CCDS28293.1; -.
DR   RefSeq; NP_031546.1; NM_007520.2.
DR   RefSeq; XP_006522942.1; XM_006522879.3.
DR   PDB; 2Z8H; X-ray; 2.50 A; A=1-135.
DR   PDBsum; 2Z8H; -.
DR   AlphaFoldDB; P97302; -.
DR   SMR; P97302; -.
DR   BioGRID; 198294; 95.
DR   DIP; DIP-46342N; -.
DR   IntAct; P97302; 28.
DR   STRING; 10090.ENSMUSP00000026703; -.
DR   iPTMnet; P97302; -.
DR   PhosphoSitePlus; P97302; -.
DR   jPOST; P97302; -.
DR   PaxDb; 10090-ENSMUSP00000026703; -.
DR   PeptideAtlas; P97302; -.
DR   ProteomicsDB; 277175; -.
DR   Pumba; P97302; -.
DR   Antibodypedia; 920; 462 antibodies from 39 providers.
DR   DNASU; 12013; -.
DR   Ensembl; ENSMUST00000026703.6; ENSMUSP00000026703.6; ENSMUSG00000025612.6.
DR   GeneID; 12013; -.
DR   KEGG; mmu:12013; -.
DR   UCSC; uc007zup.1; mouse.
DR   AGR; MGI:894680; -.
DR   CTD; 571; -.
DR   MGI; MGI:894680; Bach1.
DR   VEuPathDB; HostDB:ENSMUSG00000025612; -.
DR   eggNOG; KOG3863; Eukaryota.
DR   GeneTree; ENSGT00940000158923; -.
DR   HOGENOM; CLU_015243_2_0_1; -.
DR   InParanoid; P97302; -.
DR   OMA; RRSECPW; -.
DR   OrthoDB; 382726at2759; -.
DR   PhylomeDB; P97302; -.
DR   TreeFam; TF326681; -.
DR   Reactome; R-MMU-9707616; Heme signaling.
DR   Reactome; R-MMU-9708530; Regulation of BACH1 activity.
DR   BioGRID-ORCS; 12013; 2 hits in 114 CRISPR screens.
DR   ChiTaRS; Bach1; mouse.
DR   EvolutionaryTrace; P97302; -.
DR   PRO; PR:P97302; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; P97302; Protein.
DR   Bgee; ENSMUSG00000025612; Expressed in indifferent gonad and 283 other cell types or tissues.
DR   ExpressionAtlas; P97302; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR   GO; GO:0098531; F:ligand-activated transcription factor activity; ISO:MGI.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:0006281; P:DNA repair; ISO:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd18277; BTB_POZ_BACH1; 1.
DR   CDD; cd14719; bZIP_BACH; 1.
DR   Gene3D; 1.10.880.10; Transcription factor, Skn-1-like, DNA-binding domain; 1.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR043321; bZIP_BACH.
DR   InterPro; IPR004826; bZIP_Maf.
DR   InterPro; IPR046347; bZIP_sf.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   InterPro; IPR008917; TF_DNA-bd_sf.
DR   PANTHER; PTHR46105; AGAP004733-PA; 1.
DR   PANTHER; PTHR46105:SF1; TRANSCRIPTION REGULATOR PROTEIN BACH1; 1.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF03131; bZIP_Maf; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF47454; A DNA-binding domain in eukaryotic transcription factors; 1.
DR   SUPFAM; SSF57959; Leucine zipper domain; 1.
DR   SUPFAM; SSF54695; POZ domain; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
DR   Genevisible; P97302; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repressor; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..739
FT                   /note="Transcription regulator protein BACH1"
FT                   /id="PRO_0000076455"
FT   DOMAIN          34..100
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   DOMAIN          560..623
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          287..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          344..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          565..581
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          585..592
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          679..708
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..312
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        349..366
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        692..708
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         196
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14867"
FT   MOD_RES         448
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   HELIX           16..30
FT                   /evidence="ECO:0007829|PDB:2Z8H"
FT   STRAND          36..40
FT                   /evidence="ECO:0007829|PDB:2Z8H"
FT   STRAND          43..47
FT                   /evidence="ECO:0007829|PDB:2Z8H"
FT   HELIX           49..55
FT                   /evidence="ECO:0007829|PDB:2Z8H"
FT   HELIX           57..63
FT                   /evidence="ECO:0007829|PDB:2Z8H"
FT   STRAND          71..74
FT                   /evidence="ECO:0007829|PDB:2Z8H"
FT   HELIX           81..93
FT                   /evidence="ECO:0007829|PDB:2Z8H"
FT   TURN            100..102
FT                   /evidence="ECO:0007829|PDB:2Z8H"
FT   HELIX           103..113
FT                   /evidence="ECO:0007829|PDB:2Z8H"
FT   HELIX           116..118
FT                   /evidence="ECO:0007829|PDB:2Z8H"
FT   HELIX           119..125
FT                   /evidence="ECO:0007829|PDB:2Z8H"
SQ   SEQUENCE   739 AA;  81374 MW;  CE2DE606B05F6E32 CRC64;
     MSVSESAVFA YESSVHSTNV LLSLNDQRKK DVLCDVTVLV EGQRFRAHRS VLAACSSYFH
     SRIVGQTDAE LTVTLPEEVT VKGFEPLIQF AYTAKLILSK DNVDEVCRCV EFLSVHNIEE
     SCFQFLKFKF LDSTSEQQEC ARKKCFSSHC QKADFKFSFS EQKDLEIDEA DEFLEKKRVQ
     TPQCDSRRCQ GSVKASPPLQ DSVSQACQSL CTDKDGALAL PSLCPKYRKF QKAFGTDKIR
     TLESGVRDVH TASVQPNETS ELECFGGAQG CADLHVILKC EGMKAAMESE DTEGQDPSPQ
     CPAEQPQGTP LPQDSAGPHG LYSLSALHTY EQSGDVAFAG VQSKTVKTEK PLSRPDAQDE
     KPSENQDLYL KSSMGPKEDS SSLASEDRSS VEREVAEHLA KGFWSDICST DSPCQMQLSP
     TVAKDGPEQG YSQRRSECPW LGIRISESPE PGQRTFTTLS SVNCPFISTL SSEGCSSNLE
     IGNYDYVSEP QQEPCPYACV ISLGDDSETD TEGDSESCSA REQDCEVKLP FNAQRIISLS
     RNDFQSLLKM HKLTPEQLDC IHDIRRRSKN RIAAQRCRKR KLDCIQNLES EIEKLQSEKE
     SLLKERDHIL STLGETKQNL TGLCQQVCKE AALSPEQIQI LAKYSASDCP LSFLISEKGK
     STPDGELAFT SVFSVSDVPP TAPPPCGRGS SAASQELVQE SPPTTAAAPE QATLLEPCRQ
     SAGISDFCQQ MSDKCTTDE
//